We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1lsx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1lsx.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1lsx.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1lsx| PDB=1lsx | SCENE= }}
{{STRUCTURE_1lsx| PDB=1lsx | SCENE= }}
-
'''Crystal structure of the methylimidazole-bound BjFixL heme domain'''
+
===Crystal structure of the methylimidazole-bound BjFixL heme domain===
-
==Overview==
+
<!--
-
Structures of the Bradyrhizobium japonicum FixL heme domain have been determined in the absence and presence of specific ligands to elucidate the detailed features of its O2 sensing mechanism. The putative roles of spin-state and steric hindrance were evaluated by the structure determination of ferrous CO-bound BjFixLH and correlating its features with other ligand-bound structures. As found for NO-BjFixLH, no protein conformational change was observed in CO-BjFixLH, suggesting a more complicated mechanism than solely spin state or ligand sterics. To evaluate the role of oxidation state, the structure of the ferrous deoxy-BjFixLH was determined. The structure of deoxy-BjFixLH was found to be virtually identical to the structure of the ferric met-BjFixLH. The role of hydrogen bonding of substrates to a heme-pocket water was evaluated by determining the structure of BjFixLH bound to 1-methyl-imidazole that cannot form a hydrogen bond with this water. In this case, the heme-mediated conformational change was observed, limiting the potential importance of this interaction. Finally, the structure of cyanomet-BjFixLH was revisited to rule out concerns regarding the partial occupancy of the cyanide ligand in a previous structure. In the revised structure, Arg 220 was found to move into the heme pocket to form a hydrogen bond to the bound cyanide ligand. The implications of these results on FixL's sensing mechanism are discussed.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12390021}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12390021 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12390021}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Soltis, M]]
[[Category: Soltis, M]]
[[Category: Pas fold]]
[[Category: Pas fold]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:15:21 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:06:13 2008''

Revision as of 19:06, 2 July 2008

Image:1lsx.png

Template:STRUCTURE 1lsx

Crystal structure of the methylimidazole-bound BjFixL heme domain

Template:ABSTRACT PUBMED 12390021

About this Structure

1LSX is a Single protein structure of sequence from Bradyrhizobium japonicum. Full crystallographic information is available from OCA.

Reference

Structure-based mechanism of O2 sensing and ligand discrimination by the FixL heme domain of Bradyrhizobium japonicum., Hao B, Isaza C, Arndt J, Soltis M, Chan MK, Biochemistry. 2002 Oct 29;41(43):12952-8. PMID:12390021

Page seeded by OCA on Wed Jul 2 22:06:13 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lsx"
Personal tools